Abstract: Three batches of yogurts were made with soy protein
isolate (SPI) supplemented with 2% (S2), 4% (S4) or 6% (S6) of
skim milk powder (SMP). The fourth batch (control; S0) was
prepared from SPI without SMP supplementation. Lactobacillus
delbrueckii ssp. bulgaricus ATCC 11842 (Lb 11842) and
Streptococcus thermophilus ST 1342 (ST 1342) were used as the
starter culture. Biotransformation of the inactive forms, isoflavone
glycosides (IG) to biologically active forms, isoflavone aglycones
(IA), was determined during 28 d storage. The viability of both
microorganisms was significantly higher (P < 0.05) in S2, S4, and S6
than that in S0. The ratio of lactic acid/acetic acid in S0 was in the
range of 15.53 – 22.31 compared to 7.24 – 12.81 in S2, S4 and S6.
The biotransformation of IG to IA in S2, S4 and S6 was also
enhanced by 9.9 -13.3% compared to S0.
Abstract: Knowledge of patterns of genetic diversity enhances
the efficiency of germplasm conservation and improvement. In this
study 96 Iranian landraces of Triticum turgidum originating from
different geographical areas of Iran, along with 18 durum cultivars
from ten countries were evaluated for variation in morphological and
high molecular weight glutenin subunit (HMW-GS) composition.
The first two principal components clearly separated the Iranian
landraces from cultivars. Three alleles were present at the Glu-A1
locus and 11 alleles at Glu-B1. In both cultivars and landraces of
durum wheat, the null allele (Glu-A1c) was observed more
frequently than the Glu-A1a and Glu-A1b alleles. Two alleles,
namely Glu-B1a (subunit 7) and Glu-B1e (subunit 20) represented
the more frequent alleles at Glu-B1 locus. The results showed that
the evaluated Iranian landraces formed an interesting source of
favourable glutenin subunits that might be very desirable in breeding
activities for improving pasta-making quality.
Abstract: Biologically active peptides are of particular interest
in food science and human nutrition because they have been shown to play several physiological roles. In vitro gastrointestinal digestion of lentil and whey proteins in this study produced high angiotensin-I converting enzyme inhibitory activity with 75.5±1.9 and 91.4±2.3%
inhibition, respectively. High ACE inhibitory activity was observed in lentil after 5 days of germination (84.3±1.2%). Fractionation by
reverse phase chromatography gave inhibitory activities as high as
86.3±2.0 for lentil, 94.8±1.8% for whey and 93.7±1.7% at 5th day of germination. Further purification by HPLC resulted in several
inhibitory peptides with IC50 values ranging from 0.064 to 0.164
mg/ml. These results demonstrate that lentil proteins are a good
source of peptides with ACE inhibitory activity that can be released by germination or gastrointestinal digestion. Despite the lower bioactivity in comparison with whey proteins, incorporation of lentil proteins in functional food formulations and natural drugs look promising.